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Proliferating cell nuclear antigen (PCNA) has been shown to interact with a variety of DNA polymerases (pol) such as pol delta, pol epsilon, pol iota, pol kappa, pol eta, and pol beta. Here we show that PCNA directly interacts with the newly discovered pol lambda cloned from human cells. This interaction stabilizes the binding of pol lambda to the primer template, thus increasing its affinity for the hydroxyl primer and its processivity in DNA synthesis. However, no effect of PCNA was detected on the rate of nucleotide incorporation or discrimination efficiency by pol lambda. PCNA was found to stimulate efficient synthesis by pol lambda across an abasic (AP) site. When compared with pol delta, human pol lambda showed the ability to incorporate a nucleotide in front of the lesion. Addition of PCNA led to efficient elongation past the AP site by pol lambda but not by pol delta. However, when tested on a template containing a bulky DNA lesion, such as the major cisplatin Pt-d(GpG) adduct, PCNA could not allow translesion synthesis by pol lambda. Our results suggest that the complex between PCNA and pol lambda may play an important role in the bypass of abasic sites in human cells.

Original publication

DOI

10.1074/jbc.M206889200

Type

Journal article

Journal

J Biol Chem

Publication Date

13/12/2002

Volume

277

Pages

48434 - 48440

Keywords

Base Sequence, Cisplatin, DNA Adducts, DNA Polymerase beta, DNA Primers, DNA Repair, Electrophoretic Mobility Shift Assay, Humans, Molecular Sequence Data, Proliferating Cell Nuclear Antigen, Protein Binding, Recombinant Proteins